ID   RAPA_SHEHH              Reviewed;         968 AA.
AC   B0TVM8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=RNA polymerase-associated protein RapA {ECO:0000255|HAMAP-Rule:MF_01821};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01821};
DE   AltName: Full=ATP-dependent helicase HepA {ECO:0000255|HAMAP-Rule:MF_01821};
GN   Name=rapA {ECO:0000255|HAMAP-Rule:MF_01821}; OrderedLocusNames=Shal_3791;
OS   Shewanella halifaxensis (strain HAW-EB4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=458817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription regulator that activates transcription by
CC       stimulating RNA polymerase (RNAP) recycling in case of stress
CC       conditions such as supercoiled DNA or high salt concentrations.
CC       Probably acts by releasing the RNAP, when it is trapped or immobilized
CC       on tightly supercoiled DNA. Does not activate transcription on linear
CC       DNA. Probably not involved in DNA repair. {ECO:0000255|HAMAP-
CC       Rule:MF_01821}.
CC   -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the core
CC       RNAP than for the holoenzyme. Its ATPase activity is stimulated by
CC       binding to RNAP. {ECO:0000255|HAMAP-Rule:MF_01821}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01821}.
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DR   EMBL; CP000931; ABZ78331.1; -; Genomic_DNA.
DR   RefSeq; WP_012278849.1; NC_010334.1.
DR   AlphaFoldDB; B0TVM8; -.
DR   SMR; B0TVM8; -.
DR   STRING; 458817.Shal_3791; -.
DR   EnsemblBacteria; ABZ78331; ABZ78331; Shal_3791.
DR   KEGG; shl:Shal_3791; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; 291634at2; -.
DR   Proteomes; UP000001317; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01821; Helicase_RapA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR023949; Helicase_RapA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022737; RapA_C.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR040765; Tudor_1_RapA.
DR   InterPro; IPR040766; Tudor_2_RapA.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12137; RapA_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF18339; Tudor_1_RapA; 1.
DR   Pfam; PF18337; Tudor_RapA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Transcription; Transcription regulation.
FT   CHAIN           1..968
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000088383"
FT   DOMAIN          163..332
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          491..678
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           278..281
FT                   /note="DEAH box"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   968 AA;  109001 MW;  1BB51E39151B3691 CRC64;
     MPFSLGQRWI SDTESELGLG TVVGVEGRMV TVLFPATGEN RLFSRTEAPL TRVIYNPGDT
     IESHEEWSLV VTEVEEKDSL IIYHGTHSET GEQVSLRETL LNHNIRFNKP QDRLFAGQID
     RLDRFNVRYQ CQLLRNKLAT SDLLGLQGPR VGLIPHQQWI AHEVGQRFAP RVLLADEVGL
     GKTIEAGLII HQQLLTGRAE RILVIVPDTL RHQWLVEMLR RFNLRFSVFD EDRCVEAYAD
     NDNPFYTEQL VICSLDLLRK KRRLDQALDA DWDLMVVDEA HHLEWSEEAP SRAYQIVEAL
     SEEIPGVLLL TATPDQLGHQ SHFARLRLLD PDRFYDYQAF LKEEDSYKDV ATAADALASG
     ESLSDESIAG LTQLLSEKDI SASIALIQDD SADTDTRLQA RDELLQDLLD RHGTGRVLYR
     NSRASVKGFP QRNLHVHPQK MPEQYVTAYR VSAMMNKHLD TNAKVRQVLS PEKIYQDFDS
     GSASWWKFDP RVDWLIDFLK TNRSKKVLII ASQAETALSL EEALRTREGI QATVFHEGMS
     IIERDKAGAY FAQETGGAQA LICSEIGSEG RNFQFASNLV LFDLPLNPDL LEQRIGRLDR
     IGQKNDVEIH LPYLANTAQE RLTEWYHQGL NAFECTCPSG HILFNEFSGE LLETLLNNDE
     TSLETLLDNT KARYQELKLA MEQGRDKLLE INSHGGERAN KLVQSLADKD GDTQLIGSVI
     RLWDIIGVEQ EDSGENAIVL HPSEHMMFPT YPGLPEDGIT VTFDREMALS RDDIALITQE
     HPLVQTGLDL ITSSETGTTS VAVLKNKALP AGTIFLELIY LADASAPKSS QLYRYLPPTP
     VRVLLDKNGN NLSDNVTYES FNKQLSAVNR HIASKLVNAS QAILHPLFAK AETFANAELQ
     TLTACAREKM TSQLSGELER LKALKAVNPN IRDEELSHLS EQMSELNRYL DSSKLQLDAV
     RLVLVSHA